Evidence map›Paper›PMID 22725693›Full record

ReviewACS chemical biology2012

Fine-tuning multiprotein complexes using small molecules.

Andrea D Thompson, Amanda Dugan, Jason E Gestwicki, Anna K Mapp

Abstract readReview
In one paragraph

Review in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

59 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Review
  3. Decrypting Allostery in Membrane-Bound K-Ras4B Using ComplementaryJournal of the American Chemical Society · 2024
    Article
  4. Article
  5. Characterization ofAnalytical chemistry · 2022
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Inhibitors and chemical probes for molecular chaperone networks.The Journal of biological chemistry · 2019
    Review
  18. Review
  19. Small-molecule CaProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Andrea D ThompsonProgram in Chemical Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Amanda Dugan
Jason E Gestwicki
Anna K Mapp
University of Michigan–Ann Arbor · US

Funding

Molecular Chaperones and Small MoleculesR01NS059690 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jason E Gestwicki · 2008 to 2026
$7.9M
Probing Transcriptional Activation at the Molecular Level - Equipment SupplementR01GM065330 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MAPP, ANNA K. · 2002 to 2019
$4.2M
Targeting the ETV/PEA3 transcriptional circuitry with selective small molecule probesR01CA140667 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MAPP, ANNA K. · 2009 to 2020
$3.2M
Modulating the fate of tau in the Hsp70 chaperone system.F30AG035464 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI THOMPSON, ANDREA DOOLEY · 2009 to 2012
$90k
NCI NIH HHS R01 CA140667NCI NIH HHS R01CA140667NIA NIH HHS F30 AG035464NIA NIH HHS F30AG035464NIGMS NIH HHS GM 2R0106553NIGMS NIH HHS R01 GM065330NINDS NIH HHS R01 NS059690NINDS NIH HHS R01NS059690
6 · The paper itself

Abstract

Multiprotein complexes such as the transcriptional machinery, signaling hubs, and protein folding machines are typically composed of at least one enzyme combined with multiple non-enzymes. Often the components of these complexes are incorporated in a combinatorial manner, in which the ultimate composition of the system helps dictate the type, location, or duration of cellular activities. Although drugs and chemical probes have traditionally targeted the enzyme components, emerging strategies call for controlling the function of protein complexes by modulation of protein-protein interactions (PPIs). However, the challenges of targeting PPIs have been well documented, and the diversity of PPIs makes a "one-size-fits-all" solution highly unlikely. These hurdles are particularly daunting for PPIs that encompass large buried surface areas and those with weak affinities. In this Review, we discuss lessons from natural systems, in which allostery and other mechanisms are used to overcome the challenge of regulating the most difficult PPIs. These systems may provide a blueprint for identifying small molecules that target challenging PPIs and affecting molecular decision-making within multiprotein systems.

Indexed as

Protein Interaction MappingAllosteric SiteAnimalsDrug DesignHumansLigandsModels, MolecularMultiprotein ComplexesProtein BindingProteinsSignal TransductionTranscription, GeneticLigandsMultiprotein ComplexesProteins

Identifiers

PMID22725693
PMCPMC3517816
OpenAlexW2032313009

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.